A0A432GQJ8 · A0A432GQJ8_9DELT

  • Protein
    Glyceraldehyde-3-phosphate dehydrogenase
  • Gene
    gap
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Features

Showing features for binding site, active site, site.

Type
IDPosition(s)Description
Binding site12-13NAD+ (UniProtKB | ChEBI)
Binding site34NAD+ (UniProtKB | ChEBI)
Binding site78NAD+ (UniProtKB | ChEBI)
Binding site120NAD+ (UniProtKB | ChEBI)
Binding site152-154D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI)
Active site153Nucleophile
Site180Activates thiol group during catalysis
Binding site183D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI)
Binding site212-213D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI)
Binding site235D-glyceraldehyde 3-phosphate (UniProtKB | ChEBI)
Binding site317NAD+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular FunctionNAD binding
Molecular FunctionNADP binding
Molecular Functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Biological Processglucose metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glyceraldehyde-3-phosphate dehydrogenase
  • EC number

Gene names

    • Name
      gap
    • ORF names
      DSY93_05285
      , DSY96_03995
      , DSY98_01625

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • MAG 151
    • MAG 58
    • MAG 63_2
  • Taxonomic lineage
    Bacteria > Deltaproteobacteria > SAR324 cluster

Accessions

  • Primary accession
    A0A432GQJ8

Proteomes

Interaction

Subunit

Homotetramer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-153Glyceraldehyde 3-phosphate dehydrogenase NAD(P) binding

Sequence similarities

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    336
  • Mass (Da)
    36,093
  • Last updated
    2019-05-08 v1
  • Checksum
    C1FA54E2ED5990A1
MTIRIAINGFGRIGRMVVRAANKNQNVEIVAINDLVPSENLAYLLKYDSTHGRFDGDVQAGQDCLVVDGKTIECLSERNPGDLPWNKMNIDYVIESTGLFTTSEKAEEHLKAGAKKVVISAPAKSAEIKTLVMGVNNETYDPGTDNIVSNASCTTNCLAPIVKVVLDNYGIEEGLMTTVHSVTAAQPTVDGPSKKDWRGGRGGPQNIIPASTGAAKAVALCIPEIAGKLTGMSFRVPTPNVSVVDLTVKLSKSTSYEEINSSMKAASEGKLKGILGFTDEDVVSSDFIGSTYSSIYDAGAGIGLNDRFFKLVSWYDNEMGYSTRLIDLIEYMEGQN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QNZM01000062
EMBL· GenBank· DDBJ
RTZ82057.1
EMBL· GenBank· DDBJ
Genomic DNA
QNZK01000140
EMBL· GenBank· DDBJ
RTZ85826.1
EMBL· GenBank· DDBJ
Genomic DNA
QNZH01000148
EMBL· GenBank· DDBJ
RTZ90114.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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